Q9LBG2 (LVR_LEIAQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Levodione reductase
EC=1.1.1.-

Alternative name(s):
(6R)-2,2,6-trimethyl-1,4-cyclohexanedione reductase

Gene names

Name:

lvr

Organism

Leifsonia aquatica (Corynebacterium aquaticum)

Taxonomic identifier

144185 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Microbacteriaceae › Leifsonia

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the regio- and stereoselective reversible NAD-dependent reduction of (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol).
Catalytic activity	(4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone + NAD+ = (6R)-2,2,6-trimethyl-1,4-cyclohexanedione + NADH.
Enzyme regulation	Strongly activated by monovalent cations, such as K+, Na+, and NH4+.
Sequence similarities	Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 267

267

Levodione reductase

PRO_0000054721

Regions

Nucleotide binding

17 – 42

26

NAD

Sites

Active site

165

1

Proton acceptor

Binding site

152

1

Substrate

Site

103

1

Role in the determination of stereospecificity

Experimental info

Mutagenesis

103

1

E → A, D, N or Q: 26-fold increase in Km and a much lower enantiomeric excess of the reaction products. Ref.3

Secondary structure

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267

Helix Strand Turn

Details...

Beta strand

15 – 19

5

Turn

20 – 22

3

Helix

24 – 35

12

Beta strand

39 – 45

7

Helix

47 – 60

14

Beta strand

66 – 70

5

Helix

76 – 90

15

Beta strand

94 – 98

5

Helix

109 – 111

3

Helix

114 – 124

11

Helix

126 – 142

17

Beta strand

146 – 150

5

Helix

153 – 155

3

Beta strand

160 – 162

3

Helix

163 – 183

21

Helix

184 – 186

3

Beta strand

189 – 195

7

Helix

201 – 210

10

Helix

215 – 223

9

Helix

234 – 244

11

Helix

247 – 249

3

Beta strand

256 – 260

5

Turn

261 – 265

5

Sequences

	Sequence		Length	Mass (Da)
	Q9LBG2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6F05C89383500304	FASTA	267	27,920
	10 20 30 40 50 60 MTATSSPTTR FTDRVVLITG GGSGLGRATA VRLAAEGAKL SLVDVSSEGL EASKAAVLET 70 80 90 100 110 120 APDAEVLTTV ADVSDEAQVE AYVTATTERF GRIDGFFNNA GIEGKQNPTE SFTAAEFDKV 130 140 150 160 170 180 VSINLRGVFL GLEKVLKIMR EQGSGMVVNT ASVGGIRGIG NQSGYAAAKH GVVGLTRNSA 190 200 210 220 230 240 VEYGRYGIRI NAIAPGAIWT PMVENSMKQL DPENPRKAAE EFIQVNPSKR YGEAPEIAAV 250 260 VAFLLSDDAS YVNATVVPID GGQSAAY

References

[1]	"Cloning, sequence analysis, and expression in Escherichia coli of the gene encoding monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13." Yoshisumi A., Wada M., Takagi H., Shimizu S., Nakamori S. Biosci. Biotechnol. Biochem. 65:830-836(2001) [PubMed: 11388460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: M-13.
[2]	"Purification and characterization of monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13." Wada M., Yoshizumi A., Nakamori S., Shimizu S. Appl. Environ. Microbiol. 65:4399-4403(1999) [PubMed: 10508066] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION. Strain: M-13.
[3]	"The crystal structure and stereospecificity of levodione reductase from Corynebacterium aquaticum M-13." Sogabe S., Yoshizumi A., Fukami T.A., Shiratori Y., Shimizu S., Takagi H., Nakamori S., Wada M. J. Biol. Chem. 278:19387-19395(2003) [PubMed: 12621044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD AND INHIBITOR, MUTAGENESIS OF GLU-103. Strain: M-13.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB042262 Genomic DNA. Translation: BAA95121.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IY8	X-ray	1.60	A/B/C/D/E/F/G/H	1-267	[»]

ProteinModelPortal

Q9LBG2.

SMR

Q9LBG2. Positions 10-267.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF00106. adh_short. 1 hit.
[Graphical view]

PRINTS

PR00081. GDHRDH.
PR00080. SDRFAMILY.

ProtoNet

Search...

Entry information

Entry name

LVR_LEIAQ

Accession

Primary (citable) accession number: Q9LBG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program